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Zinc in PDB 1qv6: Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol

Enzymatic activity of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol:
1.1.1.1;

Protein crystallography data

The structure of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol, PDB code: 1qv6 was solved by L.A.Lebrun, D.-H.Park, S.Ramaswamy, B.V.Plapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 44.255, 51.115, 92.722, 91.61, 103.05, 109.90
R / Rfree (%) 15.7 / 20.3

Other elements in 1qv6:

The structure of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol (pdb code 1qv6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol, PDB code: 1qv6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1qv6

Go back to Zinc Binding Sites List in 1qv6
Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:25.7
occ:1.00
 NE2 A:HIS67 2.2 18.1 1.0
SG A:CYS174 2.2 16.1 1.0
SG A:CYS46 2.3 24.8 1.0
O1 A:24B378 2.3 16.1 1.0
CD2 A:HIS67 3.1 14.0 1.0
CE1 A:HIS67 3.2 15.6 1.0
C7 A:24B378 3.3 15.8 1.0
CB A:CYS46 3.3 17.6 1.0
CB A:CYS174 3.4 12.0 1.0
C5N A:NAD377 3.4 12.8 1.0
C6N A:NAD377 4.1 12.9 1.0
C4N A:NAD377 4.1 11.1 1.0
OG A:SER48 4.2 17.8 1.0
CG A:HIS67 4.2 11.3 1.0
ND1 A:HIS67 4.3 11.9 1.0
CB A:SER48 4.3 16.0 1.0
NH2 A:ARG369 4.5 31.4 1.0
C1 A:24B378 4.6 16.5 1.0
CA A:CYS174 4.7 12.0 1.0
CA A:CYS46 4.8 18.0 1.0
CE2 A:PHE93 4.8 10.0 1.0
OE2 A:GLU68 4.9 19.2 1.0
N A:GLY175 5.0 12.0 1.0
C A:CYS174 5.0 12.1 1.0

Zinc binding site 2 out of 4 in 1qv6

Go back to Zinc Binding Sites List in 1qv6
Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:14.6
occ:1.00
 SG A:CYS103 2.3 13.0 1.0
SG A:CYS111 2.3 13.1 1.0
SG A:CYS100 2.4 13.2 1.0
SG A:CYS97 2.4 14.9 1.0
CB A:CYS111 3.2 12.1 1.0
CB A:CYS103 3.3 14.0 1.0
CB A:CYS97 3.4 14.7 1.0
CB A:CYS100 3.5 16.2 1.0
N A:CYS97 3.5 13.3 1.0
CA A:CYS111 3.7 11.2 1.0
N A:CYS100 3.8 17.5 1.0
CA A:CYS97 3.9 15.1 1.0
N A:GLY98 3.9 16.1 1.0
N A:LEU112 4.0 12.5 1.0
N A:CYS103 4.1 14.5 1.0
CA A:CYS100 4.2 16.2 1.0
C A:CYS111 4.3 13.0 1.0
CA A:CYS103 4.3 14.3 1.0
C A:CYS97 4.3 16.3 1.0
N A:LYS99 4.5 17.8 1.0
C A:GLN96 4.6 13.7 1.0
C A:CYS100 4.8 15.8 1.0
CA A:GLN96 4.9 11.7 1.0
N A:LYS113 4.9 13.0 1.0
CG A:LYS113 4.9 18.2 1.0
O A:CYS100 4.9 15.1 1.0
CA A:GLY98 4.9 17.2 1.0
C A:LYS99 5.0 19.5 1.0

Zinc binding site 3 out of 4 in 1qv6

Go back to Zinc Binding Sites List in 1qv6
Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:27.0
occ:1.00
 O1 B:24B378 2.1 18.6 1.0
SG B:CYS174 2.2 19.7 1.0
NE2 B:HIS67 2.2 19.4 1.0
SG B:CYS46 2.3 26.4 1.0
CD2 B:HIS67 3.0 17.8 1.0
C7 B:24B378 3.1 17.9 1.0
CE1 B:HIS67 3.3 20.4 1.0
CB B:CYS46 3.3 22.2 1.0
CB B:CYS174 3.3 16.0 1.0
C5N B:NAD377 3.4 17.8 1.0
C4N B:NAD377 4.1 17.6 1.0
C6N B:NAD377 4.1 17.3 1.0
OG B:SER48 4.1 21.0 1.0
CG B:HIS67 4.2 16.5 1.0
CB B:SER48 4.2 21.1 1.0
ND1 B:HIS67 4.3 16.5 1.0
C1 B:24B378 4.5 20.4 1.0
NH2 B:ARG369 4.6 29.6 1.0
CA B:CYS174 4.7 15.4 1.0
CE2 B:PHE93 4.8 15.4 1.0
CA B:CYS46 4.8 22.2 1.0
N B:GLY175 4.8 15.2 1.0
OE2 B:GLU68 4.9 22.0 1.0
C B:CYS174 4.9 15.2 1.0

Zinc binding site 4 out of 4 in 1qv6

Go back to Zinc Binding Sites List in 1qv6
Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,4-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:17.0
occ:1.00
 SG B:CYS103 2.3 15.4 1.0
SG B:CYS97 2.3 18.4 1.0
SG B:CYS111 2.3 16.2 1.0
SG B:CYS100 2.4 17.8 1.0
CB B:CYS111 3.3 15.6 1.0
CB B:CYS103 3.3 14.5 1.0
CB B:CYS97 3.4 18.5 1.0
CB B:CYS100 3.4 20.2 1.0
N B:CYS97 3.5 16.4 1.0
CA B:CYS111 3.7 14.8 1.0
N B:CYS100 3.8 21.8 1.0
N B:GLY98 3.9 19.6 1.0
CA B:CYS97 3.9 18.7 1.0
N B:LEU112 3.9 14.8 1.0
CA B:CYS100 4.2 20.2 1.0
C B:CYS111 4.2 15.4 1.0
N B:CYS103 4.2 15.3 1.0
C B:CYS97 4.3 19.9 1.0
CA B:CYS103 4.3 15.2 1.0
N B:LYS99 4.5 22.4 1.0
C B:GLN96 4.6 17.0 1.0
C B:CYS100 4.8 19.3 1.0
N B:LYS113 4.8 16.8 1.0
CG B:LYS113 4.9 20.5 1.0
CA B:GLN96 4.9 16.7 1.0
CA B:GLY98 4.9 21.6 1.0
O B:HOH640 4.9 33.5 1.0
O B:CYS100 4.9 18.2 1.0
C B:LYS99 5.0 23.8 1.0

Reference:

L.A.Lebrun, D.-H.Park, S.Ramaswamy, B.V.Plapp. Participation of Histidine-51 in Catalysis By Horse Liver Alcohol Dehydrogenase. Biochemistry V. 43 3014 2004.
ISSN: ISSN 0006-2960
PubMed: 15023053
DOI: 10.1021/BI036103M
Page generated: Wed Dec 16 03:02:06 2020

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